Amidophosphoribosyltransferase precursor

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P28173 (PUR1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Amidophosphoribosyltransferase
Short name=ATase
EC=2.4.2.14

Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name=GPAT

Gene names

Name:	PPAT
Synonyms:	GPAT

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H₂O.
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Subunit structure	Homotetramer.
Sequence similarities	In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	4Fe-4S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Traceable author statement. Source: Reactome glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro purine nucleobase metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 11

Probable

PRO_0000029281

Chain

12 – 510

499

Amidophosphoribosyltransferase

PRO_0000029282

Regions

Domain

12 – 261

250

Glutamine amidotransferase type-2

Sites

Active site

For GATase activity By similarity

Metal binding

280

Iron-sulfur (4Fe-4S) By similarity

Metal binding

327

Magnesium By similarity

Metal binding

389

Magnesium By similarity

Metal binding

390

Magnesium By similarity

Metal binding

426

Iron-sulfur (4Fe-4S) By similarity

Metal binding

496

Iron-sulfur (4Fe-4S) By similarity

Metal binding

499

Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P28173 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: F4371FE1FEC7C744
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FASTA

510

56,257

        10         20         30         40         50         60 
MELEELGIRE ECGVFGCIAA GVWPTELDVP HVITLGLVGL QHRGQESAGI VTSDGESSQA 

        70         80         90        100        110        120 
FKVHKGMGLI NHVFNADSLK KLYVSNLGIG HTRYSTSGIS ELQNCQPFVV ETLHGKIAVA 

       130        140        150        160        170        180 
HNGELTNAVR LRRKLMRHGV GLSTSSDSEL ITQLLAFTPP LENDDTADWV ARIKNLMNET 

       190        200        210        220        230        240 
PTSYSLLIMH KDIIYAVRDP YGNRPLCIGR LIPVGDINGK GKDNSETEGW VVSSESCSFL 

       250        260        270        280        290        300 
SIGAEYYREV LPGEIVKISR YDVQTLDVVP RPEGDPSAFC IFEYVYFARP DSIFEGQMVY 

       310        320        330        340        350        360 
SVRRRCGQQL AIEAPVEADL VSTVPESATP AALGYAQKCG LPYVEVLCKN RYVGRTFIQP 

       370        380        390        400        410        420 
NMRLRQLGVA KKFGVLSDNF KGKRVVIIDD SIVRGNTISP IIKLLRESGA KEVHIRVASP 

       430        440        450        460        470        480 
PIRFPCYMGI NIPTKEELIA NRPEFHDLAN YIGADSVVYL SVEGLVSSVQ ESIKARKENE 

       490        500        510 
NSLKTQKSRV GKIGHCTACL TGDYPVELEW

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References

[1]	"Cloning and expression of avian glutamine phosphoribosylpyrophosphate amidotransferase. Conservation of a bacterial propeptide sequence supports a role for posttranslational processing." Zhou G., Dixon J.E., Zalkin H. J. Biol. Chem. 265:21152-21159(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Coexpression of two closely linked avian genes for purine nucleotide synthesis from a bidirectional promoter." Gavalas A., Dixon J.E., Brayton K.A., Zalkin H. Mol. Cell. Biol. 13:4784-4792(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-42.
[3]	Erratum Gavalas A., Dixon J.E., Brayton K.A., Zalkin H. Mol. Cell. Biol. 13:7977-7977(1993)

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60069 mRNA. Translation: AAA62736.1. L12533 Unassigned DNA. Translation: AAA17895.1.
IPI	IPI00581378.
PIR	A38337.
RefSeq	NP_001004401.1. NM_001004401.1.
UniGene	Gga.2870.
3D structure databases
ProteinModelPortal	P28173.
ModBase	Search...
Protein family/group databases
MEROPS	C44.001.
Proteomic databases
PaxDb	P28173.
PRIDE	P28173.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	422743.
KEGG	gga:422743.
Organism-specific databases
CTD	5471.
Phylogenomic databases
eggNOG	COG0034.
HOGENOM	HOG000033688.
HOVERGEN	HBG002589.
InParanoid	P28173.
KO	K00764.
OrthoDB	EOG47M1XN.
Enzyme and pathway databases
Reactome	REACT_115655. Metabolism.
UniPathway	UPA00074; UER00124.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR000836. PRibTrfase_dom. [Graphical view]
Pfam	PF00310. GATase_2. 2 hits. PF00156. Pribosyltran. 1 hit. [Graphical view]
PIRSF	PIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMs	TIGR01134. purF. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20825333.

Entry information

Entry name

PUR1_CHICK

Accession

Primary (citable) accession number: P28173

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents